ID A0A109JHS6_9BRAD Unreviewed; 578 AA.
AC A0A109JHS6;
DT 13-APR-2016, integrated into UniProtKB/TrEMBL.
DT 13-APR-2016, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE SubName: Full=Dihydroxy-acid dehydratase {ECO:0000313|EMBL:KWV48974.1};
DE EC=4.2.1.9 {ECO:0000313|EMBL:KWV48974.1};
GN ORFNames=AS156_16825 {ECO:0000313|EMBL:KWV48974.1};
OS Bradyrhizobium macuxiense.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC Nitrobacteraceae; Bradyrhizobium.
OX NCBI_TaxID=1755647 {ECO:0000313|EMBL:KWV48974.1, ECO:0000313|Proteomes:UP000057737};
RN [1] {ECO:0000313|EMBL:KWV48974.1, ECO:0000313|Proteomes:UP000057737}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BR 10303 {ECO:0000313|EMBL:KWV48974.1,
RC ECO:0000313|Proteomes:UP000057737};
RA Zelli J.E., Simoes-Araujo J.L., Barauna A.C., Silva K.;
RT "Draft Genome Sequence of the Strain BR 10303 (Bradyrhizobium sp.) isolated
RT from nodules of Centrolobium paraense.";
RL Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the IlvD/Edd family.
CC {ECO:0000256|ARBA:ARBA00006486}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KWV48974.1}.
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DR EMBL; LNCU01000104; KWV48974.1; -; Genomic_DNA.
DR RefSeq; WP_066512904.1; NZ_LNCU01000104.1.
DR AlphaFoldDB; A0A109JHS6; -.
DR OrthoDB; 7793094at2; -.
DR Proteomes; UP000057737; Unassembled WGS sequence.
DR GO; GO:0004160; F:dihydroxy-acid dehydratase activity; IEA:UniProtKB-EC.
DR GO; GO:0051536; F:iron-sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0019752; P:carboxylic acid metabolic process; IEA:UniProt.
DR GO; GO:0044238; P:primary metabolic process; IEA:UniProt.
DR Gene3D; 3.50.30.80; IlvD/EDD C-terminal domain-like; 1.
DR InterPro; IPR042096; Dihydro-acid_dehy_C.
DR InterPro; IPR000581; DiOHA_6PGluconate_deHydtase.
DR InterPro; IPR020558; DiOHA_6PGluconate_deHydtase_CS.
DR InterPro; IPR037237; IlvD/EDD_N.
DR PANTHER; PTHR43183:SF2; DIHYDROXY-ACID DEHYDRATASE; 1.
DR PANTHER; PTHR43183; HYPOTHETICAL DIHYDROXYACID DEHYDRATASE (EUROFUNG)-RELATED; 1.
DR Pfam; PF00920; ILVD_EDD; 1.
DR SUPFAM; SSF143975; IlvD/EDD N-terminal domain-like; 1.
DR SUPFAM; SSF52016; LeuD/IlvD-like; 1.
DR PROSITE; PS00886; ILVD_EDD_1; 1.
PE 3: Inferred from homology;
KW Iron {ECO:0000256|ARBA:ARBA00023004};
KW Iron-sulfur {ECO:0000256|ARBA:ARBA00023014};
KW Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000313|EMBL:KWV48974.1};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723}.
SQ SEQUENCE 578 AA; 63331 MW; 24D9940A681E4961 CRC64;
MTKNKTPDQL RSARWFAPDD LRAFGHRSRA MQMGYAPEEW RDRPVIAIIN TWSDAQPCHM
HFKSRVDDVK RGVLMAGGFP MELPALSLSE SLLKPTTMLY RNMLAMDAEE LLRGHPVDGV
VLMGGCDKTT PALLLGATSM NLPAIYLPAG PMLRGNWKGR TLGSGSDAWK YWDERRAGKI
SDKDWVDMEA GIARSYGTCM TMGTASTMTA IAESIGMTLP GASSIPAADA NHIRMSSEAG
RRIVEMVWED LTPQKIQTRQ AFENAITVAM AMGCSTNAII HLIAQARRAG QDISLDDFET
ASRKVPVIAN VRPSGDRYLM EDFFYAGGLP GLMSRIKDHL HLGCMTASGK TLGENIADAE
VYNDDVIRDV ANPIYKEGAL AVLKGNLAPD GCVIKPSACD PRFLKHTGPA LVFDDYPSMK
KAVDDPDLDV TADHVLILRN AGPQGGPGMP EWGMLPIPTK LVKQGVRDMV RLSDARMSGT
SYGACILHVS PESFIGGPLS LVRNGDRITI DVAARTINLD VPEAELAKRR AAWRAPERRF
ERGYGWMFSR HIKQANEGCD FDFLETGFGK PVGEPSIY
//